Structural Basis of the Carbohydrate Specificities of Jacalin: An X-ray and Modeling Study

• Published in: Journal of molecular biology Vol. 332; no. 1; pp. 217 - 228
• Main Authors: Arockia Jeyaprakash, A, Katiyar, S, Swaminathan, C.P, Sekar, K, Surolia, A, Vijayan, M
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 05.09.2003
• Subjects: Adjuvants, Immunologic - chemistry; Adjuvants, Immunologic - metabolism; Artocarpus - chemistry; Binding Sites; Carbohydrate Metabolism; carbohydrate specificity; Carbohydrates - chemistry; Crystallography, X-Ray; glycoproteins; Humans; Models, Molecular; Moraceae lectin; O/C–H⋯π interactions; Plant Lectins - chemistry; Plant Lectins - metabolism; Protein Binding; Protein Structure, Secondary; water bridges; O/C–H⋯π interactions; water bridges; Moraceae lectin; glycoproteins; carbohydrate specificity; XRD1, X-ray diffraction 1
• ISSN: 0022-2836; 1089-8638
• DOI: 10.1016/S0022-2836(03)00901-X

The structures of the complexes of tetrameric jacalin with Gal, Me-α-GalNAc, Me-α-T-antigen, GalNAcβ1-3Gal-α- O-Me and Galα1-6Glc (mellibiose) show that the sugar-binding site of jacalin has three components: the primary site, secondary site A, and secondary site B. In these structures and in the two structures reported earlier, Gal or GalNAc occupy the primary site with the anomeric carbon pointing towards secondary site A. The α-substituents, when present, interact, primarily hydrophobically, with secondary site A which has variable geometry. O–H⋯π and C–H⋯π hydrogen bonds involving this site also exist. On the other hand, β-substitution leads to severe steric clashes. Therefore, in complexes involving β-linked disaccharides, the reducing sugar binds at the primary site with the non-reducing end located at secondary site B. The interactions at secondary site B are primarily through water bridges. Thus, the nature of the linkage determines the mode of the association of the sugar with jacalin. The interactions observed in the crystal structures and modeling based on them provide a satisfactory qualitative explanation of the available thermodynamic data on jacalin–carbohydrate interactions. They also lead to fresh insights into the nature of the binding of glycoproteins by jacalin.